Abstract
A glycosulfatase activity toward gastric sulfomucin was identified in the extracellular material elaborated by H. pylori. The enzyme exhibited maximum activity at pH 5.7 in the presence of Triton X-100 and CaCl2, and displayed on SDS-PAGE an apparent molecular weight of 30kDa. The H. pylori glycosulfatase effectively caused desulfation of N-acetylglucosamine-6-sulfate and galactose-6-sulfate of the carbohydrate chains of mucins, as well as that of glucose-6-sulfate of glyceroglucolipids, but was ineffective towards galactosyl- and lactosylceramide sulfates which contain galactose-3-sulfate. The glycosulfatase activity towards human gastric sulfomucin was affected by an antiulcer agent, nitecapone, which at its optimal concentration (100 μg/ml) caused a 61% inhibition. The results show that H. pylori through its glycosulfatase activity causes desulfation of sulfated mucins and glyceroglucolipids of the protective mucus layer, and that nitecapone is able to interfere with this detrimental action.
Original language | American English |
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Pages (from-to) | 1091-1099 |
Number of pages | 9 |
Journal | Biochemistry International |
Volume | 26 |
Issue number | 6 |
State | Published - 1992 |
ASJC Scopus subject areas
- Biochemistry